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Structure paper

TitleStructures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent.
Journal, issue, pagesProtein Sci., Vol. 2, Page 2226-2232, Year 1993
Publish dateMay 28, 1993 (structure data deposition date)
AuthorsPjura, P. / Matthews, B.W.
External linksPubMed:8298466
MethodsX-ray diffraction
Resolution1.7 Å
Structure data

PDB-129l:
STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-130l:
STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-131l:
STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-HOH:
WATER

Source
  • enterobacteria phage t4 (virus)
KeywordsHYDROLASE(O-GLYCOSYL)

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